P0A6F5 (CH60_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60 kDa chaperonin

Alternative name(s):
GroEL protein
Protein Cpn60

Gene names

Name:	groL
Synonyms:	groEL, mopA
Ordered Locus Names:	b4143, JW4103

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. HAMAP-Rule MF_00600 Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell. HAMAP-Rule MF_00600
Subunit structure	Oligomer of 14 subunits composed of two stacked rings of 7 subunits.
Subcellular location	Cytoplasm. Note: Uniformly located in the cytoplasm (Ref.15). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (Ref.17); polar localization depends on the minCDE operon. Foci form near midcell Probable. Ref.15 Ref.17
Post-translational modification	Phosphorylated reversibly during heat shock. Ref.11
Miscellaneous	This protein shows ATPase activity. HAMAP-Rule MF_00600
Sequence similarities	Belongs to the chaperonin (HSP60) family.
Caution	Was originally (Ref.6) designated as the ams protein.
Sequence caution	The sequence AAA23934.1 differs from that shown. Reason: Frameshift at positions 424 and 455.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from mutant phenotype PubMed 2573517. Source: EcoCyc protein refolding Inferred from electronic annotation. Source: HAMAP response to heat Inferred from expression pattern PubMed 8349564. Source: EcoliWiki virion assembly Inferred from mutant phenotype PubMed 7015340. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.22. Source: EcoCyc ATPase activity Inferred from direct assay PubMed 379350. Source: EcoCyc unfolded protein binding Inferred from mutant phenotype PubMed 2573517. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-543750,EBI-543750
aceE	P0AFG8	2	EBI-543750,EBI-542683
ACT1	P60010	5	EBI-543750,EBI-2169	From a different organism.
cho	P76213	2	EBI-543750,EBI-545155
groS	P0A6F9	15	EBI-543750,EBI-369169
hyfG	P77329	3	EBI-543750,EBI-548413
malE	P0AEX9	3	EBI-543750,EBI-369910
mlaF	P63386	3	EBI-543750,EBI-561408
recF	P0A7H0	3	EBI-543750,EBI-556839
rfbC	P37745	2	EBI-543750,EBI-557071
ulaR	P0A9W0	3	EBI-543750,EBI-560926
uspG	P39177	4	EBI-543750,EBI-561722
ybbL	P77279	2	EBI-543750,EBI-560090
yhbU	P45527	3	EBI-543750,EBI-561157

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 548

547

60 kDa chaperonin HAMAP-Rule MF_00600

PRO_0000063358

Amino acid modifications

Modified residue

34

1

N6-succinyllysine Ref.16

Modified residue

51

1

N6-succinyllysine Ref.16

Modified residue

117

1

N6-acetyllysine; alternate Ref.14

Modified residue

117

1

N6-succinyllysine; alternate Ref.16

Modified residue

277

1

N6-succinyllysine Ref.16

Modified residue

321

1

N6-succinyllysine Ref.16

Modified residue

390

1

N6-succinyllysine Ref.16

Experimental info

Sequence conflict

83 – 86

4

DAAG → GALQ in CAA30739. Ref.5

Sequence conflict

262

1

L → A in CAA30698. Ref.1

Sequence conflict

267

1

M → I in CAA30698. Ref.1

Sequence conflict

343

1

Q → R in AAA23934. Ref.6

Secondary structure

1

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548

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

9 – 28

20

Beta strand

37 – 40

4

Beta strand

43 – 46

4

Beta strand

48 – 50

3

Helix

53 – 59

7

Helix

65 – 85

21

Helix

89 – 108

20

Helix

113 – 134

22

Helix

141 – 151

11

Turn

152 – 154

3

Helix

156 – 169

14

Beta strand

173 – 178

6

Beta strand

181 – 184

4

Beta strand

186 – 191

6

Beta strand

193 – 196

4

Beta strand

199 – 201

3

Helix

202 – 204

3

Turn

208 – 211

4

Beta strand

212 – 217

6

Beta strand

219 – 227

9

Helix

230 – 243

14

Beta strand

247 – 254

8

Helix

256 – 267

12

Beta strand

268 – 270

3

Beta strand

273 – 277

5

Beta strand

279 – 281

3

Helix

282 – 296

15

Beta strand

300 – 302

3

Helix

303 – 305

3

Helix

309 – 311

3

Helix

314 – 316

3

Beta strand

318 – 325

8

Beta strand

330 – 335

6

Helix

339 – 355

17

Helix

359 – 375

17

Beta strand

376 – 380

5

Helix

386 – 409

24

Beta strand

411 – 413

3

Turn

414 – 416

3

Helix

417 – 425

9

Turn

426 – 428

3

Helix

434 – 446

13

Helix

449 – 457

9

Helix

462 – 471

10

Beta strand

476 – 479

4

Turn

480 – 483

4

Beta strand

484 – 487

4

Turn

488 – 492

5

Beta strand

494 – 496

3

Helix

497 – 515

19

Beta strand

517 – 523

7

Sequences

	Sequence		Length	Mass (Da)
	P0A6F5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CD3A0FB505F74AD1	FASTA	548	57,329
	10 20 30 40 50 60 MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 70 80 90 100 110 120 ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 130 140 150 160 170 180 DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 190 200 210 220 230 240 TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 250 260 270 280 290 300 AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 310 320 330 340 350 360 ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 370 380 390 400 410 420 DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 430 440 450 460 470 480 RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 490 500 510 520 530 540 ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homologous plant and bacterial proteins chaperone oligomeric protein assembly." Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J. Nature 333:330-334(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria." Miki T., Orita T., Furuno M., Horiuchi T. J. Mol. Biol. 201:327-338(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
[6]	"Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli." Chanda P.K., Ono M., Kuwano M., Kung H.-F. J. Bacteriol. 161:446-449(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22. Strain: K12 / EMG2.
[8]	Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"A role of RnlA in the RNase LS activity from Escherichia coli." Otsuka Y., Koga M., Iwamoto A., Yonesaki T. Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-10. Strain: K12.
[10]	"The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde ATP." Thomson G.J., Coggins J.R., Price N.C. FEBS Lett. 336:19-22(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 455-519.
[11]	"Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation." Sherman M.Y., Goldberg A.L. Nature 357:167-169(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[12]	"Residues in chaperonin GroEL required for polypeptide binding and release." Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Nature 371:614-619(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[13]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[14]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[15]	"Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing." Winkler J., Seybert A., Konig L., Pruggnaller S., Haselmann U., Sourjik V., Weiss M., Frangakis A.S., Mogk A., Bukau B. EMBO J. 29:910-923(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"Identification of lysine succinylation as a new post-translational modification." Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y. Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-34; LYS-51; LYS-117; LYS-277; LYS-321 AND LYS-390. Strain: K12.
[17]	"Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli." Li G., Young K.D. Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[18]	"The crystal structure of the bacterial chaperonin GroEL at 2.8 A." Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B. Nature 371:578-586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[19]	"Conformational variability in the refined structure of the chaperonin GroEL at 2.8-A resolution." Braig K., Adams P.D., Bruenger A.T. Nat. Struct. Biol. 2:1083-1094(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[20]	"The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S." Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B. Nat. Struct. Biol. 3:170-177(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[21]	"Chaperone activity and structure of monomeric polypeptide binding domains of GroEL." Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R. Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[22]	"The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex." Xu Z., Horwich A.L., Sigler P.B. Nature 388:741-750(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[23]	"The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity." Chen L., Sigler P.B. Cell 99:757-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
[24]	"Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions." Kiser P.D., Lodowski D.T., Palczewski K. Acta Crystallogr. F 63:457-461(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07850 Genomic DNA. Translation: CAA30698.1.
U14003 Genomic DNA. Translation: AAA97042.1.
U00096 Genomic DNA. Translation: AAC77103.1.
AP009048 Genomic DNA. Translation: BAE78145.1.
X07899 Genomic DNA. Translation: CAA30739.1.
M11294 Genomic DNA. Translation: AAA23934.1. Frameshift.

PIR

BVECGL. S56371.

RefSeq

NP_418567.1. NC_000913.2.
YP_492286.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AON	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1DK7	X-ray	2.02	A/B	191-336	[»]
1DKD	X-ray	2.10	A/B/C/D	191-336	[»]
1FY9	X-ray	2.20	A	191-376	[»]
1FYA	X-ray	2.20	A	191-376	[»]
1GR5	electron microscopy	7.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1GRL	X-ray	2.80	A/B/C/D/E/F/G	1-548	[»]
1GRU	electron microscopy	12.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1J4Z	X-ray	3.52	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1JON	X-ray	2.50	A	191-345	[»]
1KID	X-ray	1.70	A	191-375	[»]
1KP8	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1KPO	X-ray	3.52	1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z	2-547	[»]
1LA1	X-ray	2.06	A	188-379	[»]
1MNF	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1OEL	X-ray	2.80	A/B/C/D/E/F/G	2-548	[»]
1PCQ	X-ray	2.81	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1PF9	X-ray	2.99	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-525	[»]
1SS8	X-ray	2.70	A/B/C/D/E/F/G	2-524	[»]
1SVT	X-ray	2.81	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1SX3	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-525	[»]
1SX4	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1XCK	X-ray	2.92	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
2C7C	electron microscopy	7.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2C7D	electron microscopy	8.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2C7E	electron microscopy	9.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
2CGT	electron microscopy	8.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2EU1	X-ray	3.29	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
2NWC	X-ray	3.02	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
2YEY	X-ray	3.30	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-525	[»]
3C9V	electron microscopy	4.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-527	[»]
3CAU	electron microscopy	4.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-527	[»]
4AAQ	electron microscopy	8.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
4AAR	electron microscopy	8.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
4AAS	electron microscopy	8.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
4AAU	electron microscopy	8.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
4AB2	electron microscopy	8.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
4AB3	electron microscopy	8.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]

ProteinModelPortal

P0A6F5.

SMR

P0A6F5. Positions 2-525.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-339N.

IntAct

P0A6F5. 691 interactions.

MINT

MINT-5232496.

STRING

511145.b4143.

2D gel databases

SWISS-2DPAGE

P0A6F5.

Proteomic databases

PaxDb

P0A6F5.

PRIDE

P0A6F5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77103; AAC77103; b4143.
BAE78145; BAE78145; BAE78145.

GeneID

12934083.
948665.

KEGG

ecj:Y75_p4030.
eco:b4143.

PATRIC

32123855. VBIEscCol129921_4275.

Organism-specific databases

EchoBASE

EB0594.

EcoGene

EG10599. groL.

Phylogenomic databases

eggNOG

COG0459.

HOGENOM

HOG000076290.

KO

K04077.

OMA

YNGVITV.

ProtClustDB

PRK00013.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10599-MONOMER.
ECOL316407:JW4103-MONOMER.

SABIO-RK

P0A6F5.

Gene expression databases

Genevestigator

P0A6F5.

Family and domain databases

HAMAP

MF_00600. CH60.

InterPro

IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
[Graphical view]

PANTHER

PTHR11353. PTHR11353. 1 hit.

Pfam

PF00118. Cpn60_TCP1. 1 hit.
[Graphical view]

PRINTS

PR00298. CHAPERONIN60.

SUPFAM

SSF48592. GroEL-ATPase. 1 hit.

TIGRFAMs

TIGR02348. GroEL. 1 hit.

PROSITE

PS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6F5.

Entry information

Entry name

CH60_ECOLI

Accession

Primary (citable) accession number: P0A6F5
Secondary accession number(s): P06139, Q2M6G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program